ACTN_ACTCC
ID ACTN_ACTCC Reviewed; 380 AA.
AC P00785; A0A2R6QY08; A0A3G9DHM4; E5D7U1; E5D7U2; Q9AXD2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 5.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Actinidain;
DE Short=Actinidin;
DE EC=3.4.22.14;
DE AltName: Allergen=Act c 1;
DE Flags: Precursor;
GN Name=ACT1A {ECO:0000303|PubMed:22039217};
GN ORFNames=CEY00_Acc12058 {ECO:0000312|EMBL:PSS17271.1};
OS Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=1590841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=22039217; DOI=10.1104/pp.111.187989;
RA Nieuwenhuizen N.J., Maddumage R., Tsang G.K., Fraser L.G., Cooney J.M.,
RA De Silva H.N., Green S., Richardson K.A., Atkinson R.G.;
RT "Mapping, complementation, and targets of the cysteine protease actinidin
RT in kiwifruit.";
RL Plant Physiol. 158:376-388(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX DOI=10.2503/hortj.OKD-133;
RA Kamiyoshihara Y., Nakamura T., Itagaki Y., Asada S., Aoki T., Mizuno S.,
RA Watanabe K., Inoue H., Tateishi A.;
RT "Differential constitution in promoter region leads to a phenotype with a
RT lower allergic actinidin level in yellow-fleshed kiwifruit (Actinidia
RT chinensis).";
RL Hort. J. 87:288-296(2018).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee N.K., Hahm Y.T.;
RT "Isolation and expression in E. coli of actinidin gene from Chinese wild
RT kiwifruit.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Red5;
RX PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT highlights the challenges associated with draft genomes and gene prediction
RT in plants.";
RL BMC Genomics 19:257-257(2018).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-380, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX AGRICOLA=IND92000625; DOI=10.1007/BF00027396;
RA Praekelt U.M., McKee R.A., Smith H.;
RT "Molecular analysis of actinidin, the cysteine proteinase of Actinidia
RT chinesis.";
RL Plant Mol. Biol. 10:193-202(1988).
RN [6]
RP PROTEIN SEQUENCE OF 127-346.
RX PubMed=687380; DOI=10.1042/bj1730073;
RA Carne A., Moore C.H.;
RT "The amino acid sequence of the tryptic peptides from actinidin, a
RT proteolytic enzyme from the fruit of Actinidia chinensis.";
RL Biochem. J. 173:73-83(1978).
RN [7]
RP PROTEIN SEQUENCE OF 127-136, AND FUNCTION.
RC STRAIN=cv. Hort 16A; TISSUE=Fruit;
RX PubMed=18442249; DOI=10.1021/jf703620m;
RA Tuppo L., Giangrieco I., Palazzo P., Bernardi M.L., Scala E., Carratore V.,
RA Tamburrini M., Mari A., Ciardiello M.A.;
RT "Kiwellin, a modular protein from green and gold kiwi fruits: evidence of
RT in vivo and in vitro processing and IgE binding.";
RL J. Agric. Food Chem. 56:3812-3817(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=7003158; DOI=10.1016/0022-2836(80)90255-7;
RA Baker E.N.;
RT "Structure of actinidin, after refinement at 1.7-A resolution.";
RL J. Mol. Biol. 141:441-484(1980).
CC -!- FUNCTION: Cysteine protease responsible for the cleavage of kiwellin
CC into kissper and KiTH. {ECO:0000269|PubMed:18442249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity close to that of papain.; EC=3.4.22.14;
CC -!- TISSUE SPECIFICITY: Fruit. {ECO:0000269|Ref.5}.
CC -!- DEVELOPMENTAL STAGE: Levels of mRNA accumulate during early fruit
CC development. {ECO:0000269|Ref.5}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31435.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA31529.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; GU201520; ADQ85985.1; -; Genomic_DNA.
DR EMBL; GU201528; ADQ85986.1; -; mRNA.
DR EMBL; LC330913; BBA83994.1; -; Genomic_DNA.
DR EMBL; AF343446; AAK06862.1; -; mRNA.
DR EMBL; NKQK01000011; PSS17271.1; -; Genomic_DNA.
DR EMBL; X13013; CAA31435.1; ALT_FRAME; mRNA.
DR EMBL; X13139; CAA31529.1; ALT_FRAME; mRNA.
DR PDB; 1AEC; X-ray; 1.86 A; A=127-344.
DR PDB; 2ACT; X-ray; 1.70 A; A=127-346.
DR PDBsum; 1AEC; -.
DR PDBsum; 2ACT; -.
DR AlphaFoldDB; P00785; -.
DR SMR; P00785; -.
DR Allergome; 1; Act d 1.
DR Allergome; 3052; Act d 1.0101.
DR MEROPS; C01.007; -.
DR MEROPS; I29.003; -.
DR EnsemblPlants; PSS17271; PSS17271; CEY00_Acc12058.
DR Gramene; PSS17271; PSS17271; CEY00_Acc12058.
DR BRENDA; 3.4.22.14; 120.
DR EvolutionaryTrace; P00785; -.
DR Proteomes; UP000241394; Chromosome lg11.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..126
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:18442249,
FT ECO:0000269|PubMed:687380"
FT /id="PRO_0000026398"
FT CHAIN 127..380
FT /note="Actinidain"
FT /id="PRO_0000026399"
FT ACT_SITE 151
FT ACT_SITE 288
FT ACT_SITE 308
FT DISULFID 148..191
FT DISULFID 182..224
FT DISULFID 282..332
FT CONFLICT 27
FT /note="A -> T (in Ref. 1; ADQ85985)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="D -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="S -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="Q -> R (in Ref. 1; ADQ85985/ADQ85986)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="G -> S (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..170
FT /note="VTGV -> TSGS (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="D -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="R -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193..194
FT /note="VG -> GS (in Ref. 1; ADQ85986)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="V -> G (in Ref. 1; ADQ85985)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="Q -> P (in Ref. 1; ADQ85986)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="E -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="E -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="V -> L (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..231
FT /note="NE -> DQ (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> G (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="H -> Q (in Ref. 1; ADQ85985/ADQ85986)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="S -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="I -> T (in Ref. 1; ADQ85985/ADQ85986)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..291
FT /note="VT -> IV (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="I -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="K -> E (in Ref. 5; CAA31435)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="H -> Y (in Ref. 5; CAA31435/CAA31529)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="P -> S (in Ref. 5; CAA31435/CAA31529)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="N -> K (in Ref. 1; ADQ85985)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> E (in Ref. 5; CAA31435/CAA31529)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="D -> H (in Ref. 5; CAA31529)"
FT /evidence="ECO:0000305"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:2ACT"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:2ACT"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2ACT"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:2ACT"
SQ SEQUENCE 380 AA; 42098 MW; C2DA505454525B93 CRC64;
MGLPKSFVSM SLLFFSTLLI LSLAFNAKNL TQRTNDEVKA MYESWLIKYG KSYNSLGEWE
RRFEIFKETL RFIDEHNADT NRSYKVGLNQ FADLTDEEFR STYLGFTSGS NKTKVSNQYE
PRVGQVLPSY VDWRSAGAVV DIKSQGECGG CWAFSAIATV EGINKIVTGV LISLSEQELI
DCGRTQNTRG CNVGYITDGF QFIINNGGIN TEENYPYTAQ DGECNVDLQN EKYVTIDTYE
NVPYNNEWAL QTAVTYQPVS VALDAAGDAF KHYSSGIFIG PCGTAIDHAV TIVGYGTEGG
IDYWIVKNSW DTTWGEEGYM RILRNVGGAG TCGIATMPSY PVKYNNQNHP KSYSSLINPP
AFSMSNDGPV GVDDGQRYSA
